BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34139

Title: LysF1 sh3b domain structure   PubMed: 28852930

Authors: Benesik, M.; Novacek, J.; Janda, L.; Dopitova, R.; Pernisova, M.; Melkova, K.; Tisakova, L.; Doskar, J.; Zidek, L.; Hejatko, J.; Pantucek, R.

Citation: Benesik, M.; Novacek, J.; Janda, L.; Dopitova, R.; Pernisova, M.; Melkova, K.; Tisakova, L.; Doskar, J.; Zidek, L.; Hejatko, J.; Pantucek, R.. "Role of SH3b binding domain in a natural deletion mutant of Kayvirus endolysin LysF1 with a broad range of lytic activity."  Virus Genes ., .-. (2017).

Assembly members:
entity_1, polymer, 106 residues, 11530.995 Da.

Natural source:   Common Name: Kayvirus   Taxonomy ID: 1857843   Superkingdom: Viruses   Kingdom: not available   Genus/species: Kayvirus not available

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: ETPATRPVTGSWKKNQYGTW YKPENATFVNGNQPIVTRIG SPFLNAPVGGNLPAGATIVY DEVCIQAGHIWIGYNAYNGN RVYCPVRTCQGVPPNQIPGV AWGVFK

Data sets:
Data typeCount
13C chemical shifts439
15N chemical shifts111
1H chemical shifts695

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 106 residues - 11530.995 Da.

1   GLUTHRPROALATHRARGPROVALTHRGLY
2   SERTRPLYSLYSASNGLNTYRGLYTHRTRP
3   TYRLYSPROGLUASNALATHRPHEVALASN
4   GLYASNGLNPROILEVALTHRARGILEGLY
5   SERPROPHELEUASNALAPROVALGLYGLY
6   ASNLEUPROALAGLYALATHRILEVALTYR
7   ASPGLUVALCYSILEGLNALAGLYHISILE
8   TRPILEGLYTYRASNALATYRASNGLYASN
9   ARGVALTYRCYSPROVALARGTHRCYSGLN
10   GLYVALPROPROASNGLNILEPROGLYVAL
11   ALATRPGLYVALPHELYS

Samples:

sample_1: Na-phosphate 20 mM; sh3b domain, [U-99% 13C; U-99% 15N], 0.25 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNH NOESYsample_1isotropicsample_conditions_1
3D HCH NOESYsample_1isotropicsample_conditions_1
3D HCH NOESYsample_1isotropicsample_conditions_1
1D Hsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceII 600 MHz
  • Bruker AvanceII 950 MHz

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